PDBsum entry 2if4

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Signaling protein PDB id
Protein chain
258 a.a.
Waters ×16

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Key reference
Title Crystal structure of a multi-Domain immunophilin from arabidopsis thaliana: a paradigm for regulation of plant abc transporters.
Authors J.Granzin, A.Eckhoff, O.H.Weiergräber.
Ref. J Mol Biol, 2006, 364, 799-809. [DOI no: 10.1016/j.jmb.2006.09.052]
PubMed id 17045295
FKBP42 is a membrane-anchored immunophilin playing a critical role in morphogenesis and development of higher plants. We present the X-ray structure of the cytoplasmic portion of FKBP42 comprising both the FKBP-like domain and the TPR domain at 2.85 A resolution. The data shed light on the probable binding modes of key interaction partners, including HSP90 and two classes of ABC transporters. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
Figure 1.
Figure 1. Ribbon representation of the AtFKBP42(1–339) crystal structure determined here. The mean B factors per residue are indicated by a color gradient from white (mean B < 35 Å^2) to red (mean B > 90 Å^2). Side-chains involved in hydrogen bonds at the domain interface are drawn in stick mode. Hydrophobic contacts (see the text) are omitted for clarity.
Figure 2.
Figure 2. Proposed interaction of AtFKBP42 with the C terminus of AtHSP90. (a) Superposition of AtFKBP42(1–339) (FKBP-like domain in red, TPR domain in orange) with the TPR2A module of HOP (grey) complexed with the MEEVD peptide (green). (b) Close-up view of the side-chain interactions of HOP-TPR2A with MEEVD, along with the corresponding residues in the TPR domain of AtFKBP42 (colored as in (a)). Residues of AtFKBP42 are numbered in orange, those of the MEEVD peptide in black.
The above figures are reprinted by permission from Elsevier: J Mol Biol (2006, 364, 799-809) copyright 2006.
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